Please use this identifier to cite or link to this item: https://doi.org/10.1023/A:1018461131484
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dc.titleThe Cys-rich and EGF-like domains of Carcinoscorpius rotundicauda Factor C yields soluble fusion protein with GFP
dc.contributor.authorDwarakanath, R.S.
dc.contributor.authorHo, B.
dc.contributor.authorDing, J.L.
dc.date.accessioned2014-10-27T08:42:08Z
dc.date.available2014-10-27T08:42:08Z
dc.date.issued1997
dc.identifier.citationDwarakanath, R.S.,Ho, B.,Ding, J.L. (1997). The Cys-rich and EGF-like domains of Carcinoscorpius rotundicauda Factor C yields soluble fusion protein with GFP. Biotechnology Letters 19 (11) : 1147-1150. ScholarBank@NUS Repository. <a href="https://doi.org/10.1023/A:1018461131484" target="_blank">https://doi.org/10.1023/A:1018461131484</a>
dc.identifier.issn01415492
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101890
dc.description.abstractThe expression of the different domains of a complex serine protease, recombinant Factor C of the horseshoe crab, Carcinoscorpius rotundicauda, was achieved using pClneo and pEGFP-N1 vectors. In an in vitro coupled transcription-translation assay, the truncated CrFC cDNA insert coding for the initial 331 amino acids expressed the expected 36 kDa polypeptide lacking the antigenic epitopes. The highly disulfide-bonded Cys-rich and EGF-like domains at the N-terminus of CrFC which bind LPS were fused to GFP. When expressed in COS-1 cells, this fusion protein did not alter the localisation of the chromophore and remained soluble, indicating that other domains could be responsible for the membrane-bound nature of the recombinant Factor C, rFC. The expression of this LPS-binding domain of rFC as a soluble protein suggests possibilities of obtaining active rFC in mammalian cells.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1023/A:1018461131484
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1023/A:1018461131484
dc.description.sourcetitleBiotechnology Letters
dc.description.volume19
dc.description.issue11
dc.description.page1147-1150
dc.description.codenBILED
dc.identifier.isiutNOT_IN_WOS
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